title: The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica).
abstract: The complete amino acid sequence of a major trypsin inhibitor (FMTI-II) from seeds of foxtail millet (Setaria italica) was determined by analysis of peptides derived from the reduced and S-carboxymethylated protein by digestion with TPCK-trypsin and Staphylococcus aureus V8 protease. FMTI-II consists of 67 amino acid residues, including 10 half-cystine residues which are involved in 5 disulfide bridges in the molecule. The established sequence had a high degree of homology to Bowman-Birk type inhibitors from leguminous and gramineous plants. The trypsin reactive-site peptide bond in FMTI-II also appears to be Lys (16)-Ser (17) by comparison with these sequences.
authors.affiliation: Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University.
authors.forename: M
authors.initials: M
authors.lastname: Tashiro
authors.forename: T
authors.initials: T
authors.lastname: Asao
authors.forename: C
authors.initials: C
authors.lastname: Hirata
authors.forename: K
authors.initials: K
authors.lastname: Takahashi
authors.forename: M
authors.initials: M
authors.lastname: Kanamori
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry*; D006109:Poaceae; D012639:Seeds / Q000032:analysis* / Q000187:drug effects; D012697:Serine Endopeptidases / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
chemical_list: C067589:FMTI-II protein, Setaria italica; D010940:Plant Proteins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin